TY  - JOUR
AU  - Österlund, Nicklas
AU  - Kulkarni, Yashraj S.
AU  - Misiaszek, Agata D.
AU  - Wallin, Cecilia
AU  - Krüger, Dennis M.
AU  - Liao, Qinghua
AU  - Mashayekhy Rad, Farshid
AU  - Jarvet, Jüri
AU  - Strodel, Birgit
AU  - Wärmländer, Sebastian K. T. S.
AU  - Ilag, Leopold L.
AU  - Kamerlin, Shina C. L.
AU  - Gräslund, Astrid
TI  - Amyloid-β Peptide Interactions with Amphiphilic Surfactants: Electrostatic and Hydrophobic Effects
JO  - ACS chemical neuroscience
VL  - 9
IS  - 7
SN  - 1948-7193
CY  - Washington, DC
PB  - ACS Publ.
M1  - FZJ-2018-07744
SP  - 1680 - 1692
PY  - 2018
AB  - The amphiphilic nature of the amyloid-β (Aβ) peptide associated with Alzheimer's disease facilitates various interactions with biomolecules such as lipids and proteins, with effects on both structure and toxicity of the peptide. Here, we investigate these peptide-amphiphile interactions by experimental and computational studies of Aβ(1-40) in the presence of surfactants with varying physicochemical properties. Our findings indicate that electrostatic peptide-surfactant interactions are required for coclustering and structure induction in the peptide and that the strength of the interaction depends on the surfactant net charge. Both aggregation-prone peptide-rich coclusters and stable surfactant-rich coclusters can form. Only Aβ(1-40) monomers, but not oligomers, are inserted into surfactant micelles in this surfactant-rich state. Surfactant headgroup charge is suggested to be important as electrostatic peptide-surfactant interactions on the micellar surface seems to be an initiating step toward insertion. Thus, no peptide insertion or change in peptide secondary structure is observed using a nonionic surfactant. The hydrophobic peptide-surfactant interactions instead stabilize the Aβ monomer, possibly by preventing self-interaction between the peptide core and C-terminus, thereby effectively inhibiting the peptide aggregation process. These findings give increased understanding regarding the molecular driving forces for Aβ aggregation and the peptide interaction with amphiphilic biomolecules.
LB  - PUB:(DE-HGF)16
C6  - pmid:29683649
UR  - <Go to ISI:>//WOS:000439531400017
DO  - DOI:10.1021/acschemneuro.8b00065
UR  - https://juser.fz-juelich.de/record/858908
ER  -